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Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1.

http://www.ncbi.nlm.nih.gov/pubmed/11154276

The Akt family of serine/threonine-directed kinases promotes cellular survival in part by phosphorylating and inhibiting death-inducing proteins. Here we describe a novel functional interaction between Akt and apoptosis signal-regulating kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase. Akt decreased ASK1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus Akt site at serine 83 of ASK1. Activation of the phosphoinositide 3-kinase (PI3-K)/Akt pathway also inhibited the serum deprivation-induced activity of endogenous ASK1 in L929 cells. An association between Akt and ASK1 was detected in cells by coimmunoprecipitation. Phosphorylation by Akt inhibited ASK1-mediated c-Jun N-terminal kinase and activating transcription factor 2 activities in intact cells. Finally, activation of the PI3-K/Akt pathway reduced apoptosis induced by ASK1 in a manner dependent on phosphorylation of serine 83 of ASK1. These results provide the first direct link between Akt and the family of stress-activated kinases.

Pubmed ID: 11154276 RIS Download

Mesh terms: Amino Acid Sequence | Apoptosis | Cell Line | Cell Survival | HeLa Cells | Humans | JNK Mitogen-Activated Protein Kinases | MAP Kinase Kinase Kinase 5 | MAP Kinase Kinase Kinases | Mitogen-Activated Protein Kinases | Phosphatidylinositol 3-Kinases | Phosphorylation | Protein-Serine-Threonine Kinases | Proto-Oncogene Proteins | Proto-Oncogene Proteins c-akt | Serine | Signal Transduction | Substrate Specificity

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